Molecular mechanism of constitutively active Rab11A was revealed by crystal structure of Rab11A S20V.

about

Molecular mechanism of constitutively active Rab11A was revealed by crystal structure of Rab11A S20V.

Item

http://www.wikidata.org/entity/Q53171820

description

2016 nî lūn-bûn

@nan

2016年の論文

@ja

2016年学术文章

@wuu

2016年学术文章

@zh

2016年学术文章

@zh-cn

2016年学术文章

@zh-hans

2016年学术文章

@zh-my

2016年学术文章

@zh-sg

2016年學術文章

@yue

2016年學術文章

@zh-hant

name

Molecular mechanism of constit ...... stal structure of Rab11A S20V.

@en

Molecular mechanism of constit ...... stal structure of Rab11A S20V.

@nl

type

Item

label

Molecular mechanism of constit ...... stal structure of Rab11A S20V.

@en

Molecular mechanism of constit ...... stal structure of Rab11A S20V.

@nl

prefLabel

Molecular mechanism of constit ...... stal structure of Rab11A S20V.

@en

Molecular mechanism of constit ...... stal structure of Rab11A S20V.

@nl

P1476

Molecular mechanism of constit ...... stal structure of Rab11A S20V.

@en

P2093

Chang Min Kim

http://www.w3.org/2001/XMLSchema#string

Hyun Ho Park

http://www.w3.org/2001/XMLSchema#string

Jae Young Choi

http://www.w3.org/2001/XMLSchema#string

Jong Hwan Yoon

http://www.w3.org/2001/XMLSchema#string

Ju-Hong Jeon

http://www.w3.org/2001/XMLSchema#string

Jun Hyuck Lee

http://www.w3.org/2001/XMLSchema#string

Young-Cheul Shin

http://www.w3.org/2001/XMLSchema#string

P2860

Crystallographic evidence for substrate-assisted GTP hydrolysis by a small GTP binding protein

Family-wide characterization of the DENN domain Rab GDP-GTP exchange factors

The crystal structure of the small GTPase Rab11b reveals critical differences relative to the Rab11a isoform

Structural basis of family-wide Rab GTPase recognition by rabenosyn-5

A Rab11-containing rapidly recycling compartment in macrophages that promotes phagocytosis

Rab11 regulates recycling through the pericentriolar recycling endosome

PROCHECK: a program to check the stereochemical quality of protein structures

Processing of X-ray diffraction data collected in oscillation mode

Functional changes in the structure of the SRP GTPase on binding GDP and Mg2+GDP

An open conformation of switch I revealed by the crystal structure of a Mg2+-free form of RHOA complexed with GDP. Implications for the GDP/GTP exchange mechanism

P304

819-827

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1002/1873-3468.12100

http://www.w3.org/2001/XMLSchema#string

P407

English

P433

http://www.w3.org/2001/XMLSchema#string

P478

590

http://www.w3.org/2001/XMLSchema#string

P577

2016-03-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

26879265

http://www.w3.org/2001/XMLSchema#string